Belmont SURFS

Dbp5-Nup159 Multicopy Suppression Screen and Confirmation to Identify Nuclear and Cytoplasmic Dbp5 Targets

The export of mature mRNA through the nuclear pore is a vital step in the process of making proteins in eukaryotic cells such as budding yeast cell S. cerevisiae. RNA binding proteins (RBPs) such as Mex67 attach to mature mRNA to enable exit through the nuclear pore complex (NPC). Once escorted through the NPC, Dbp5 detaches Mex67 from the mRNA to provide directionality to RNA transport in a process called RNA remodeling. While Dbp5 has this known function at the NPC, it is also found in the nucleus and cytoplasm where its function is not yet known. I hypothesize that Dbp5 works to remove other RBPs from RNA in the nucleus or cytoplasm. To test this hypothesis, I performed a multicopy suppressor screen to identify proteins that could rescue the growth defects of a Dbp5-nup159 fusion strain which lacks the function of Dbp5 in the cytoplasm and nucleus. Through this screen I identified several proteins that could be potential targets for Dbp5 remodeling in the cytoplasm or nucleus and hope to confirm and sequence these results in the future.